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    KCNK1 potassium two pore domain channel subfamily K member 1 [ Homo sapiens (human) ]

    Gene ID: 3775, updated on 18-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Evidence for an Association Between a pH-Dependent Potassium Channel, TWIK-1, and the Accuracy of Smooth Pursuit Eye Movements.

    Evidence for an Association Between a pH-Dependent Potassium Channel, TWIK-1, and the Accuracy of Smooth Pursuit Eye Movements.
    Bargary G, Bosten JM, Lawrance-Owen AJ, Goodbourn PT, Mollon JD., Free PMC Article

    08/14/2024
    KCNK1 promotes proliferation and metastasis of breast cancer cells by activating lactate dehydrogenase A (LDHA) and up-regulating H3K18 lactylation.

    KCNK1 promotes proliferation and metastasis of breast cancer cells by activating lactate dehydrogenase A (LDHA) and up-regulating H3K18 lactylation.
    Hou X, Ouyang J, Tang L, Wu P, Deng X, Yan Q, Shi L, Fan S, Fan C, Guo C, Liao Q, Li Y, Xiong W, Li G, Zeng Z, Wang F., Free PMC Article

    07/10/2024
    Overexpressed KCNK1 regulates potassium channels affecting molecular mechanisms and biological pathways in bladder cancer.

    Overexpressed KCNK1 regulates potassium channels affecting molecular mechanisms and biological pathways in bladder cancer.
    Zhang W, Chen XS, Wei Y, Wang XM, Chen XJ, Chi BT, Huang LQ, He RQ, Huang ZG, Li Q, Chen G, He J, Wu M., Free PMC Article

    05/2/2024
    Identification of KCNK1 as a potential prognostic biomarker and therapeutic target of breast cancer.

    Identification of KCNK1 as a potential prognostic biomarker and therapeutic target of breast cancer.
    Sun X, Li Y, Lan H, Jiang T, Wan X, Cheng Y.

    02/4/2023
    Selectivity filter instability dominates the low intrinsic activity of the TWIK-1 K2P K(+) channel.

    Selectivity filter instability dominates the low intrinsic activity of the TWIK-1 K2P K(+) channel.
    Nematian-Ardestani E, Abd-Wahab F, Chatelain FC, Sun H, Schewe M, Baukrowitz T, Tucker SJ., Free PMC Article

    09/19/2020
    Dynamics of the TWIK-1 Channel

    Exploring the Dynamics of the TWIK-1 Channel.
    Oakes V, Furini S, Pryde D, Domene C., Free PMC Article

    06/24/2017
    Our data indicate that TWIK-1 has a highly conserved role in cardiac function and is required for normal heart rate and atrial morphology. Despite the functional importance of TWIK-1 in the atrium, genetic variation in KCNK1 is not a common primary cause of human AF.

    The two-pore domain potassium channel, TWIK-1, has a role in the regulation of heart rate and atrial size.
    Christensen AH, Chatelain FC, Huttner IG, Olesen MS, Soka M, Feliciangeli S, Horvat C, Santiago CF, Vandenberg JI, Schmitt N, Olesen SP, Lesage F, Fatkin D.

    06/3/2017
    TWIK-1 protein possesses a hydrophobic barrier deep within the inner pore

    A hydrophobic barrier deep within the inner pore of the TWIK-1 K2P potassium channel.
    Aryal P, Abd-Wahab F, Bucci G, Sansom MS, Tucker SJ., Free PMC Article

    11/21/2015
    Potassium channels, in particular K2P channels, are expressed and functional in the apical membrane of airway epithelial cells

    A role for two-pore K⁺ channels in modulating Na⁺ absorption and Cl⁻ secretion in normal human bronchial epithelial cells.
    Zhao KQ, Xiong G, Wilber M, Cohen NA, Kreindler JL., Free PMC Article

    02/25/2012
    study presents the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1; an extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals

    Crystal structure of the human two-pore domain potassium channel K2P1.
    Miller AN, Long SB.

    02/11/2012
    ion selectivity of TWIK-1 K+ channels during pathological hypokalemia; a molecular basis for inward leak Na+ currents that could trigger or contribute to cardiac paradoxical depolarization in lowered [K+]o; mechanism for regulating cardiac excitability.

    TWIK-1 two-pore domain potassium channels change ion selectivity and conduct inward leak sodium currents in hypokalemia.
    Ma L, Zhang X, Chen H.

    11/26/2011
    TWIK1 is internalized via a dynamin-dependent mechanism and addressed to the recycling endosomal compartment. Mutation in its cytoplasmic C terminus (I293A,I294A) stabilizes TWIK1 at the plasma membrane, resulting in robust currents.

    Potassium channel silencing by constitutive endocytosis and intracellular sequestration.
    Feliciangeli S, Tardy MP, Sandoz G, Chatelain FC, Warth R, Barhanin J, Bendahhou S, Lesage F., Free PMC Article

    05/31/2010
    Observational study of gene-disease association, gene-gene interaction, gene-environment interaction, and genetic testing. (HuGE Navigator)

    Integrative predictive model of coronary artery calcification in atherosclerosis.
    McGeachie M, Ramoni RL, Mychaleckyj JC, Furie KL, Dreyfuss JM, Liu Y, Herrington D, Guo X, Lima JA, Post W, Rotter JI, Rich S, Sale M, Ramoni MF., Free PMC Article

    04/7/2010
    support TWIK-1 and TREK-1 as being the major components of the long-sought K(+) channels underlying the passive conductance of mature hippocampal astrocytes

    TWIK-1 and TREK-1 are potassium channels contributing significantly to astrocyte passive conductance in rat hippocampal slices.
    Zhou M, Xu G, Xie M, Zhang X, Schools GP, Ma L, Kimelberg HK, Chen H., Free PMC Article

    01/21/2010
    Removal of the peptide adduct by SUMO protease reveals K2P1 to be a K+-selective, pH-sensitive, openly rectifying channel regulated by reversible peptide linkage.

    Sumoylation silences the plasma membrane leak K+ channel K2P1.
    Rajan S, Plant LD, Rabin ML, Butler MH, Goldstein SA.

    01/21/2010
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